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- W1985440166 abstract "The structures of inactive mutants D144A and E78Q of the glycoside hydrolase family 8 (GH-8) endo-beta-1,4-d-xylanase (pXyl) from the Antarctic bacterium Pseudoalteromonas haloplanktis TAH3a in complex with its substrate xylopentaose (at 1.95 A resolution) and product xylotriose (at 1.9 A resolution) have been determined by X-ray crystallography. A detailed comparative analysis of these with the apo-enzyme and with other GH-8 structures indicates an induced fit mechanism upon ligand binding whereby a number of conformational changes and, in particular, a repositioning of the proton donor into a more catalytically competent position occurs. This has also allowed for the description of protein-ligand interactions in this enzyme and for the demarcation of subsites -3 to +3. An in-depth analysis of each of these subsites gives an insight into the structure-function relationship of this enzyme and the basis of xylose/glucose discrimination in family 8 glycoside hydrolases. Furthermore, the structure of the -1/+1 subsite spanning complex reveals that the substrate is distorted from its ground state conformation. Indeed, structural analysis and in silico docking studies indicate that substrate hydrolysis in GH-8 members is preceded by a conformational change, away from the substrate ground-state chair conformation, to a pretransition state local minimum (2)S(O) conformation." @default.
- W1985440166 created "2016-06-24" @default.
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- W1985440166 date "2006-03-25" @default.
- W1985440166 modified "2023-10-17" @default.
- W1985440166 title "Oligosaccharide Binding in Family 8 Glycosidases: Crystal Structures of Active-Site Mutants of the β-1,4-Xylanase pXyl from<i> Pseudoaltermonas haloplanktis</i> TAH3a in Complex with Substrate and Product<sup>,</sup>" @default.
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- W1985440166 doi "https://doi.org/10.1021/bi052193e" @default.
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